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Q9KGN8

- IMDH_BACHD

UniProt

Q9KGN8 - IMDH_BACHD

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

    Catalytic activityi

    Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

    Cofactori

    Potassium.UniRule annotation

    Enzyme regulationi

    Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei249 – 2491NADUniRule annotation
    Metal bindingi301 – 3011Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi303 – 3031Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei304 – 3041IMPUniRule annotation
    Active sitei306 – 3061Thioimidate intermediateUniRule annotation
    Metal bindingi306 – 3061Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei414 – 4141IMPUniRule annotation
    Metal bindingi468 – 4681Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi469 – 4691Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi470 – 4701Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi299 – 3013NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciBHAL272558:GJC5-23-MONOMER.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    Name:guaBUniRule annotation
    Ordered Locus Names:BH0020
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 485485Inosine-5'-monophosphate dehydrogenasePRO_0000093690Add
    BLAST

    Proteomic databases

    PRIDEiQ9KGN8.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272558.BH0020.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KGN8.
    SMRiQ9KGN8. Positions 2-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 15460CBS 1UniRule annotationAdd
    BLAST
    Domaini155 – 21561CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni339 – 3413IMP bindingUniRule annotation
    Regioni362 – 3632IMP bindingUniRule annotation
    Regioni386 – 3905IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG6GTZPV.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9KGN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWENKFQKEG LTFDDVLLVP AKSEVLPRDV SVKTKLTETL QLNIPIISAG    50
    MDTVTEAKMA IAIAREGGLG IIHKNMSVEE QAEQVDRVKR SESGVITNPF 100
    FLTPDRQVFD AEHLMGKYRI SGVPIVDEDQ KLVGILTNRD LRFIEDYSTL 150
    IDDVMTKENL VTAPVGTTLK EAEEILQKHK IEKLPLVDES GTLKGLITIK 200
    DIEKVIEFPN SAKDSQGRLI VGAAVGVSAD TDVRVAALVE AGVDVIVIDT 250
    AHGHSKGVLE KVKAIREQYP DLTIIAGNVA TAEATRDLIE AGANVVKVGI 300
    GPGSICTTRI VAGIGVPQIT AVYDCANEAR KHGVPIIADG GIKYSGDIVK 350
    ALAAGGHAVM LGSLLAGVSE SPGEREIFQG RQFKVYRGMG SLGAMEKGSK 400
    DRYFQENNQK LVPEGIEGRI PYKGPLHDTI HQLVGGIRAG MGYCGTKTID 450
    ELRENTQFIR ITGAGLRESH PHDVQITKEA PNYTL 485
    Length:485
    Mass (Da):52,429
    Last modified:October 1, 2000 - v1
    Checksum:iD0B64489E5CF8B60
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB03739.1.
    PIRiD83652.
    RefSeqiNP_240886.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB03739; BAB03739; BAB03739.
    GeneIDi890466.
    KEGGibha:BH0020.
    PATRICi18936854. VBIBacHal18977_0021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB03739.1 .
    PIRi D83652.
    RefSeqi NP_240886.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali Q9KGN8.
    SMRi Q9KGN8. Positions 2-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH0020.

    Proteomic databases

    PRIDEi Q9KGN8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB03739 ; BAB03739 ; BAB03739 .
    GeneIDi 890466.
    KEGGi bha:BH0020.
    PATRICi 18936854. VBIBacHal18977_0021.

    Phylogenomic databases

    eggNOGi COG0517.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci BHAL272558:GJC5-23-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiIMDH_BACHD
    AccessioniPrimary (citable) accession number: Q9KGN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3